Lenka Záveská Drábková, Oldřich Janiczek, Ivana Davidová, Martin Mandl
Abstract
Characterization of tetrathionate hydrolase was desribed with relation to pH and temperature of the reaction. Sulfate ions strongly influenced the enzyme activity and stabilty. The molecular mass was 105 kDa. The dimer was composed from identical subunits.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
Characterization of tetrathionate hydrolase was desribed with relation to pH and temperature of the reaction. Sulfate ions strongly influenced the enzyme activity and stabilty. The molecular mass was 105 kDa. The dimer was composed from identical subunits.
Key concepts: Tetrathionate, Acidithiobacillus ferrooxidans, Chemistry, Acidithiobacillus, Dimer, Sulfate, Enzyme, Sulfur